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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
45
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pubmed:dateCreated |
1998-12-10
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pubmed:databankReference |
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pubmed:abstractText |
Signaling through the insulin receptor tyrosine kinase involves its autophosphorylation in response to insulin and the subsequent tyrosine phosphorylation of substrate proteins such as insulin receptor substrate-1 (IRS-1). In basal 3T3-L1 adipocytes, IRS-1 is predominantly membrane-bound, and this localization may be important in targeting downstream signaling elements that mediate insulin action. Since IRS-1 localization to membranes may occur through its association with specific membrane proteins, a 3T3-F442A adipocyte cDNA expression library was screened with non-tyrosine-phosphorylated, baculovirus-expressed IRS-1 in order to identify potential IRS-1 receptors. A cDNA clone that encodes sigma3A, a small subunit of the AP-3 adaptor protein complex, was demonstrated to bind IRS-1 utilizing this cloning strategy. The specific interaction between IRS-1 and sigma3A was further verified by in vitro binding studies employing baculovirus-expressed IRS-1 and a glutathione S-transferase (GST)-sigma3A fusion protein. IRS-1 and sigma3A were found to co-fractionate in a detergent-resistant population of low density membranes isolated from basal 3T3-L1 adipocytes. Importantly, the addition of exogenous purified GST-sigma3A to low density membranes caused the release of virtually all of the IRS-1 bound to these membranes, while GST alone had no effect. These results are consistent with the hypothesis that sigma3A serves as an IRS-1 receptor that may dictate the subcellular localization and the signaling functions of IRS-1.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AP3S1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex 3,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex sigma...,
http://linkedlifedata.com/resource/pubmed/chemical/Ap3s1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IRS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Irs1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Irs1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29942-9
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9792713-3T3 Cells,
pubmed-meshheading:9792713-Adaptor Protein Complex 3,
pubmed-meshheading:9792713-Adaptor Protein Complex sigma Subunits,
pubmed-meshheading:9792713-Adipocytes,
pubmed-meshheading:9792713-Amino Acid Sequence,
pubmed-meshheading:9792713-Animals,
pubmed-meshheading:9792713-Base Sequence,
pubmed-meshheading:9792713-Binding Sites,
pubmed-meshheading:9792713-Carrier Proteins,
pubmed-meshheading:9792713-Cells, Cultured,
pubmed-meshheading:9792713-Humans,
pubmed-meshheading:9792713-Insulin,
pubmed-meshheading:9792713-Insulin Receptor Substrate Proteins,
pubmed-meshheading:9792713-Mice,
pubmed-meshheading:9792713-Molecular Sequence Data,
pubmed-meshheading:9792713-Nerve Tissue Proteins,
pubmed-meshheading:9792713-Phosphoproteins,
pubmed-meshheading:9792713-Rats,
pubmed-meshheading:9792713-Rats, Inbred F344,
pubmed-meshheading:9792713-Recombinant Proteins,
pubmed-meshheading:9792713-Signal Transduction
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pubmed:year |
1998
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pubmed:articleTitle |
Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes.
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pubmed:affiliation |
Program in Molecular Medicine and the Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01605, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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